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Figure 3.
Figure 3 Flap conformational changes induced by binding of TL-3
to wild-type HIV PR. In the absence of substrate or inhibitor,
the flap regions of wild-type HIV PR adopt two distinct
conformations: `open' (rose) and `curled' (green). While the
flap regions lack interactions in the `open' conformation, a
stabilizing packing interaction is formed between the side
chains of Phe53 and Ile50' of twofold-related monomers in the
`curled' conformation. Upon binding of TL-3 (cyan), the flaps
shift toward the active site and their interactions are
reconfigured: the side chain of Phe53 now interacts with the P4
benzyl group of TL-3 (light blue) and Ile50 contacts Ile54'.
TL-3 also induces a shift in the 80s loop, which moves towards
the inhibitor such that Pro81' and Val82' contact the P1 benzyl
group.
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